PARALLEL INDUCTION OF d -ARABITOL AND d -SORBITOL DEHYDROGENASES

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Abstract
Scolnick, Edward M. (Harvard Medical School, Boston, Mass.) and Edmund C. C. Lin . Parallel induction of d -arabitol and d -sorbitol dehydrogenases. J. Bacteriol. 84: 631–637. 1962.—Two inducible diphosphopyridine nucleotide-linked dehydrogenases are described in a bacterium isolated from the soil, Cellvibrio polyoltrophicus ATCC 14774. The first enzyme catalyzes the dehydrogenation of d -arabitol to d -xylulose and d -mannitol to d -fructose. The data suggest that in vivo this enzyme has the dual function of the utilization of both of these polyhydric alcohols. The second enzyme was found to act only on d -sorbitol, converting it to d -fructose. Evidence for its physiological function as a d -sorbitol dehydrogenase is also given. Both of these enzymes were found to be induced in parallel by any of the three polyhydric alcohols, d -arabitol, d -mannitol, and d -sorbitol. A common stereoconfiguration of the inducers for these enzymes is suggested. The parallel evolution of substrate specificity and inducer specificity is discussed with respect to the functional advantage that such a selective process might offer.